View source for 5vj8


==Backbone structure of the Yersinia pestis outer membrane protein Ail in phospholipid bilayer nanodisc==
<StructureSection load='5vj8' size='340' side='right'caption='[[5vj8]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5vj8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VJ8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VJ8 FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5vj8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vj8 OCA], [https://pdbe.org/5vj8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vj8 RCSB], [https://www.ebi.ac.uk/pdbsum/5vj8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vj8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A5P8YI02_YERPE A0A5P8YI02_YERPE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Yersinia pestis the causative agent of plague, is highly pathogenic and poses very high risk to public health. The outer membrane protein Ail (Adhesion invasion locus) is one of the most highly expressed proteins on the cell surface of Y. pestis, and a major target for the development of medical countermeasures. Ail is essential for microbial virulence and is critical for promoting the survival of Y. pestis in serum. Structures of Ail have been determined by X-ray diffraction and solution NMR spectroscopy, but the protein's activity is influenced by the detergents in these samples, underscoring the importance of the surrounding environment for structure-activity studies. Here we describe the backbone structure of Ail, determined in lipid bilayer nanodiscs, using solution NMR spectroscopy. We also present solid-state NMR data obtained for Ail in membranes containing lipopolysaccharide (LPS), a major component of the bacterial outer membranes. The protein in lipid bilayers, adopts the same eight-stranded beta-barrel fold observed in the crystalline and micellar states. The membrane composition, however, appears to have a marked effect on protein dynamics, with LPS enhancing conformational order and slowing down the (15)N transverse relaxation rate. The results provide information about the way in which an outer membrane protein inserts and functions in the bacterial membrane.

Structural Insights into the Yersinia pestis Outer Membrane Protein Ail in Lipid Bilayers.,Dutta SK, Yao Y, Marassi FM J Phys Chem B. 2017 Aug 17;121(32):7561-7570. doi: 10.1021/acs.jpcb.7b03941. Epub, 2017 Aug 4. PMID:28726410<ref>PMID:28726410</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5vj8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Yersinia pestis]]
[[Category: Dutta SK]]
[[Category: Marassi FM]]
[[Category: Yong Y]]